4e61

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[[Image:4e61.png|left|200px]]
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==Crystal structure of the EB1-like motif of Bim1p==
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<StructureSection load='4e61' size='340' side='right' caption='[[4e61]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4e61]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E61 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E61 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BIM1, YER016W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])</td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4e61 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e61 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4e61 RCSB], [http://www.ebi.ac.uk/pdbsum/4e61 PDBsum]</span></td></tr>
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<table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Mitosis begins with the tethering of chromosomes to the mitotic spindle and their orientation perpendicular to the axis of cell division. In budding yeast, mitotic spindle orientation and the subsequent chromosome segregation are two independent processes. Early spindle orientation is driven by the actin-bound myosin Myo2p, which interacts with the adapter Kar9p. The latter also binds to microtubule-associated Bim1p, thereby connecting both types of cytoskeleton. This study focuses on the interaction between Kar9p and Bim1p and its regulation. We solved the crystal structure of the previously reported Kar9p-binding motif of Bim1p and identified a second, novel Kar9p-interaction domain. We further show that two independent posttranslational modification events regulate their interaction. Whereas Kar9p sumoylation is required for efficient complex formation with Bim1p, Aurora B/Ipl1p-dependent phosphorylation of Bim1p down-regulates their interaction. The observed effects of these modifications allow us to propose a novel regulatory framework for the assembly and disassembly of the early spindle-orientation complex.
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Posttranslational modifications regulate assembly of the early spindle-orientation complex in yeast.,Huls D, Storchova Z, Niessing D J Biol Chem. 2012 Mar 29. PMID:22461628<ref>PMID:22461628</ref>
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The line below this paragraph, containing "STRUCTURE_4e61", creates the "Structure Box" on the page.
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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or leave the SCENE parameter empty for the default display.
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{{STRUCTURE_4e61| PDB=4e61 | SCENE= }}
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===Crystal structure of the EB1-like motif of Bim1p===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<references/>
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The line below this paragraph, {{ABSTRACT_PUBMED_22461628}}, adds the Publication Abstract to the page
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__TOC__
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(as it appears on PubMed at http://www.pubmed.gov), where 22461628 is the PubMed ID number.
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</StructureSection>
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{{ABSTRACT_PUBMED_22461628}}
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==About this Structure==
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[[4e61]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E61 OCA].
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==See Also==
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*[[Major Histocompatibility Complex Class I|Major Histocompatibility Complex Class I]]
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==Reference==
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<ref group="xtra">PMID:022461628</ref><references group="xtra"/>
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Huels, D.]]
[[Category: Huels, D.]]

Revision as of 07:50, 5 June 2014

Crystal structure of the EB1-like motif of Bim1p

4e61, resolution 2.45Å

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